1WUW

Crystal Structure of beta hordothionin

Summary for 1WUW

• Entry DOI: 10.2210/pdb1wuw/pdb
• Descriptor: Beta-hordothionin, PARA-TOLUENE SULFONATE, SERINE, ... (4 entities in total)
• Functional Keywords: crambin fold, dimer, plant protein
• Biological source: Hordeum vulgare
• Cellular location: Secreted : P21742
• Total number of polymer chains: 2
• Total formula weight: 10428.48

Authors

Johnson, K.A.,Kim, E.,Teeter, M.M.,Suh, S.W.,Stec, B. (deposition date: 2004-12-09, release date: 2005-01-11, Last modification date: 2024-11-06)

Primary citation

Johnson, K.A.,Kim, E.,Teeter, M.M.,Suh, S.W.,Stec, B.
Crystal structure of alpha-hordothionin at 1.9 Angstrom resolution.
Febs Lett., 579:2301-2306, 2005

PubMed Abstract: Crystal structure of ubiquitous toxin from barley alpha-hordothionin (alpha-HT) has been determined at 1.9A resolution by X-ray crystallography. The primary sequence as well as the NMR solution structure of alpha-HT firmly established that alpha-HT belongs to a family of membrane active plant toxins-thionins. Since alpha-HT crystallized in a space group (P4(1)2(1)2) that is different from the space group (I422) of previously determined alpha(1)- and beta-purothionins, and visocotoxin A3, therefore, it provided independent information on protein-protein interactions that may be relevant to the toxin mechanism. The structure of alpha-HT not only confirms overall architectural features (crambin fold) but also provides an additional confirmation of the role for crucial solute molecules, that were postulated to be directly involved in the mechanism of toxicity for thionins.

PubMed: 15848162
DOI: 10.1016/j.febslet.2004.12.100

Experimental method

X-RAY DIFFRACTION (1.9 Å)